Structure of the mouse calpain small subunit gene

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1388, Issue 1, 1998, Pages 247-252

  Arthur, J Simon C ^a   Greer, Peter A ^a   Elce, John S ^a  

^a QUEEN S UNIVERSITY   (Canada)

Author keywords

Calpain; cDNA; Gene; Mouse; Small subunit

Indexed keywords

CALPAIN; COMPLEMENTARY DNA; PROTEIN SUBUNIT; TRANSCRIPTION FACTOR SP1;

ANIMAL CELL; BINDING SITE; DNA SEQUENCE; EXON; GENE STRUCTURE; MOLECULAR CLONING; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROMOTER REGION; SHORT SURVEY; TATA BOX;

EID: 0032517264     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(98)00166-6     Document Type: Article

References (19)

1. Croall D.E., DeMartino G.N. Calcium activated neutral protease (calpain) system: structure-function and regulation. Physiol. Rev. 71:1991;813-847.
2. Suzuki K., Sorimachi H., Yoshizawa T., Kinbara K., Ishiura S. Calpain: novel family members, activation and physiological function. Biol. Chem. Hoppe-Seyler. 376:1995;523-529.
3. Wang K.K.W., Yuen P.W. Calpain inhibition: an overview of its therapeutic potential. Trends Pharmacol. Sci. 15:1994;412-419.
4. Arthur J.S.C., Crawford C. Investigation of the interaction of calpain with phospholipids. Biochim. Biophys. Acta. 1293:1996;201-206.
5. Imajoh S., Kawasaki H., Suzuki K. The amino terminal hydrophobic region of the calcium-activated neutral protease (CANP) is essential for its activation by phosphatidylinositol. J. Biochem. 99:1986;1281-1284.
6. Vilei E.M., Calderara S., Anagli J., Berardi S., Hitomi K., Maki M., Carafoli E. Functional properties of recombinant calpain I and mutants lacking domains III and IV of the catalytic subunit. J. Biol. Chem. 272:1997;25802-25808.
7. Yoshizawa T., Sorimachi H., Tomioka S., Ishiura S., Suzuki K. A catalytic subunit of calpain possesses full catalytic activity. FEBS Lett. 358:1995;101-103.
8. Zhang W., Mellgren R.L. Calpain subunits remain associated during catalysis. Biochem. Biophys. Res. Commun. 227:1996;891-896.
9. Elce J.S., Davies P.L., Hegadorn C., Maurice D.H., Arthur J.S.C. The effects of truncation of the small subunit on m-calpain activity and heterodimer formation. Biochem. J. 326:1997;31-38.
10. Emori Y., Kawasaki H., Imajoh S., Kawashima S., Suzuki K. Isolation and sequence analysis of cDNA clones for the small subunit of rabbit calcium-dependent protease. J. Biol. Chem. 261:1986;9472-9476.
11. McCelland P., Lash J.A., Hathaway D.R. Identification of major autolytic cleavage sites in the regulatory subunit of vascular calpain; a comparison of partial amino-terminal sequences to deduced sequence from complementary DNA. J. Biol. Chem. 264:1989;17428-17431.
12. Ohno S., Emori Y., Suzuki K. Nucleotide sequence of a cDNA coding for the small subunit of human calcium-dependent protease. Nucleic Acids Res. 14:1986;5559.
13. 2+ binding protein: structure of the light subunit of porcine calpain elucidated by molecular cloning and protein sequence analysis. Proc. Natl. Acad. Sci. U.S.A. 82:1985;6075-6079.
14. Sorimachi H., Amano S., Ishiura S., Suzuki K. Primary sequences of rat μ-calpain large and small subunits are respectively, moderately and highly similar to those of human. Biochim. Biophys. Acta. 1309:1996;37-41.
15. Miyake M., Emori Y., Suzuki K. Gene organisation of the small subunit of human calcium-activated neutral protease. Nucleic Acids Res. 14:1986;8805-8817.
16. Ben-David Y., Letwin K., Tannock L., Bernstein A., Pawson T. A mammalian protein kinase with potential for serine/threonine and tyrosine phosphorylation is related to cell cycle regulators. EMBO J. 10:1991;317-325.
17. Weis L., Reinberg D. Accurate positioning of RNA polymerase II on a natural TATA-less promoter is independent of TATA-binding-protein-associated factors and initiator-binding proteins. Mol. Cell. Biol. 17:1997;2973-2984.
18. Hata A., Ohno S., Akita Y., Suzuki K. Tandomly reiterated negative enhancer-like elements regulate transcription of a human gene for the large subunit of calpain-dependent protease. J. Biol. Chem. 264:1989;6404-6411.
19. 2+-induced conformational changes. Nat. Struct. Biol. 4:1997;532-538.